2mb5

HYDRATION IN PROTEIN CRYSTALS. A NEUTRON DIFFRACTION ANALYSIS OF CARBONMONOXYMYOGLOBIN

Method: NEUTRON DIFFRACTION Dmax: 58.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

MYOGLOBIN

Physeter catodon

UniProt P02185

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–153 Not recorded SO4 SULFATE ION × 1 ND4 AMMONIUM CATION WITH D × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CMO CARBON MONOXIDE × 1 NEUTRON DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

354 other PDB entries and 366 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYG_PHYCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 1–153

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2mb5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mb5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2mb5
Deposition date deposition_date1989-10-11
Structure title titleHYDRATION IN PROTEIN CRYSTALS. A NEUTRON DIFFRACTION ANALYSIS OF CARBONMONOXYMYOGLOBIN
Keywords keywordsOXYGEN STORAGE; OXYGEN STORAGE
Experimental Method methodNEUTRON DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.38
Radius of gyration Rg (electron density) rg_electron15.70
Forward intensity I(0) i06190710.00
Molecular weight molecular_weight20393.0 kDa
Excluded volume excluded_volume26200 ų
Envelope volume envelope_volume31014 ų
Hydration-shell volume shell_volume15992 ų
Envelope diameter envelope_diameter59.9
Shell Rg shell_rg22.37
Envelope Rg envelope_rg16.53
Shape Rg shape_rg16.18
Total Rg total_rg15.36
Total atoms total_atoms2840
Residues n_residues153
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax58.2
Rg (real space) rg_real17.28
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real6.1910e+06
I(0) uncertainty (real space) i0_real_error7.1630e+04
Rg (reciprocal space) rg_reciprocal17.29
I(0) (reciprocal space) i0_reciprocal6191000.0000
Solution quality estimate total_estimate0.7950
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.299
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1566000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2mb5a_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.2 — Globins

CATH v4.4 (1 domains)

Domain ID domain_id2mb5A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily10 — Globins

8. Citations (9)

9. Files and Curves (10)